ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Tyrosine-protein phosphatase non-receptor type 23

Intramolecular
Cysteine 144 and cysteine 188
Cysteine 65 and cysteine 149
Cysteine 144 and cysteine 149
A redox-regulated disulphide may form within Tyrosine-protein phosphatase non-receptor type 23 between cysteines 144 and 188. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
5mjz
Structure name
crystal structure of the his domain protein tyrosine phosphatase (hd- ptp/ptpn23) bro1 domain (apo structure)
Structure deposition date
2016-12-02
Thiol separation (Å)
6
Half-sphere exposure sum ?
84
Minimum pKa ?
11
% buried
96
Peptide accession
Q9H3S7
Residue number A
144
Residue number B
188
Peptide name
Tyrosine-protein phosphatase non-receptor type 23

Ligandability

Cysteine 144 of Tyrosine-protein phosphatase non-receptor type 23

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 188 of Tyrosine-protein phosphatase non-receptor type 23

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Tyrosine-protein phosphatase non-receptor type 23 between cysteines 65 and 149. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
5mjz
Structure name
crystal structure of the his domain protein tyrosine phosphatase (hd- ptp/ptpn23) bro1 domain (apo structure)
Structure deposition date
2016-12-02
Thiol separation (Å)
8
Half-sphere exposure sum ?
78
Minimum pKa ?
11
% buried
78
Peptide accession
Q9H3S7
Residue number A
65
Residue number B
149
Peptide name
Tyrosine-protein phosphatase non-receptor type 23

Ligandability

Cysteine 65 of Tyrosine-protein phosphatase non-receptor type 23

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 149 of Tyrosine-protein phosphatase non-receptor type 23

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Tyrosine-protein phosphatase non-receptor type 23 between cysteines 144 and 149. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
23
PDB code
5mk3
Structure name
crystal structure of the his domain protein tyrosine phosphatase (hd- ptp/ptpn23) bro 1 domain (chmp4c peptide complex structure)
Structure deposition date
2016-12-02
Thiol separation (Å)
10
Half-sphere exposure sum ?
91
Minimum pKa ?
11
% buried
96
Peptide accession
Q9H3S7
Residue number A
144
Residue number B
149
Peptide name
Tyrosine-protein phosphatase non-receptor type 23

Ligandability

Cysteine 144 of Tyrosine-protein phosphatase non-receptor type 23

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 149 of Tyrosine-protein phosphatase non-receptor type 23

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

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